Fluorine in PDB 2k1q: uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor
Other elements in 2k1q:
The structure of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor
(pdb code 2k1q). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the
uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor, PDB code: 2k1q:
Jump to Fluorine binding site number:
1;
2;
Fluorine binding site 1 out
of 2 in 2k1q
Go back to
Fluorine Binding Sites List in 2k1q
Fluorine binding site 1 out
of 2 in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F190
b:0.0
occ:1.00
|
FG1
|
B:OBF190
|
0.0
|
0.0
|
1.0
|
CG
|
B:OBF190
|
1.3
|
0.0
|
1.0
|
HG
|
B:OBF190
|
2.0
|
0.0
|
1.0
|
FG2
|
B:OBF190
|
2.2
|
0.0
|
1.0
|
CB
|
B:OBF190
|
2.4
|
0.0
|
1.0
|
H1B
|
B:OBF190
|
2.5
|
0.0
|
1.0
|
HB3
|
A:LEU135
|
2.6
|
0.0
|
1.0
|
HA
|
A:LYS136
|
2.6
|
0.0
|
1.0
|
H2B
|
B:OBF190
|
2.9
|
0.0
|
1.0
|
HE2
|
A:PHE154
|
3.0
|
0.0
|
1.0
|
O
|
A:LEU135
|
3.1
|
0.0
|
1.0
|
C
|
A:LEU135
|
3.1
|
0.0
|
1.0
|
HG2
|
A:LYS136
|
3.2
|
0.0
|
1.0
|
N
|
A:LYS136
|
3.2
|
0.0
|
1.0
|
HB3
|
A:ALA157
|
3.3
|
0.0
|
1.0
|
CA
|
A:LYS136
|
3.3
|
0.0
|
1.0
|
HD3
|
A:LYS136
|
3.4
|
0.0
|
1.0
|
HZ
|
A:PHE154
|
3.5
|
0.0
|
1.0
|
CB
|
A:LEU135
|
3.5
|
0.0
|
1.0
|
CA
|
B:OBF190
|
3.6
|
0.0
|
1.0
|
HD2
|
A:LYS136
|
3.7
|
0.0
|
1.0
|
HA
|
B:OBF190
|
3.7
|
0.0
|
1.0
|
H
|
A:LYS136
|
3.7
|
0.0
|
1.0
|
CD
|
A:LYS136
|
3.8
|
0.0
|
1.0
|
HB2
|
A:LEU135
|
3.9
|
0.0
|
1.0
|
CE2
|
A:PHE154
|
3.9
|
0.0
|
1.0
|
CG
|
A:LYS136
|
3.9
|
0.0
|
1.0
|
CA
|
A:LEU135
|
3.9
|
0.0
|
1.0
|
O
|
A:VAL132
|
4.1
|
0.0
|
1.0
|
HB1
|
A:ALA157
|
4.1
|
0.0
|
1.0
|
CZ
|
A:PHE154
|
4.1
|
0.0
|
1.0
|
CB
|
A:ALA157
|
4.2
|
0.0
|
1.0
|
N
|
B:OBF190
|
4.3
|
0.0
|
1.0
|
CB
|
A:LYS136
|
4.3
|
0.0
|
1.0
|
H
|
A:ALA157
|
4.3
|
0.0
|
1.0
|
H
|
A:GLY137
|
4.4
|
0.0
|
1.0
|
C
|
A:LYS136
|
4.5
|
0.0
|
1.0
|
H
|
A:SER138
|
4.5
|
0.0
|
1.0
|
OG
|
A:SER138
|
4.5
|
0.0
|
1.0
|
O
|
B:LEU189
|
4.7
|
0.0
|
1.0
|
HG
|
A:SER138
|
4.7
|
0.0
|
1.0
|
HN
|
B:OBF190
|
4.7
|
0.0
|
1.0
|
C
|
B:LEU189
|
4.7
|
0.0
|
1.0
|
CG
|
A:LEU135
|
4.7
|
0.0
|
1.0
|
HA
|
A:LEU135
|
4.7
|
0.0
|
1.0
|
HD22
|
A:LEU135
|
4.7
|
0.0
|
1.0
|
HB2
|
A:ALA157
|
4.8
|
0.0
|
1.0
|
HG2
|
B:GLU188
|
4.8
|
0.0
|
1.0
|
O
|
B:GLU188
|
4.8
|
0.0
|
1.0
|
HD21
|
A:LEU135
|
4.8
|
0.0
|
1.0
|
N
|
A:GLY137
|
4.8
|
0.0
|
1.0
|
C
|
B:OBF190
|
4.8
|
0.0
|
1.0
|
HG
|
A:LEU135
|
4.8
|
0.0
|
1.0
|
N
|
A:ALA157
|
4.8
|
0.0
|
1.0
|
N
|
A:LEU135
|
4.8
|
0.0
|
1.0
|
HA
|
A:ALA156
|
4.9
|
0.0
|
1.0
|
HG3
|
A:LYS136
|
4.9
|
0.0
|
1.0
|
H
|
A:LEU135
|
4.9
|
0.0
|
1.0
|
HB2
|
A:LYS136
|
4.9
|
0.0
|
1.0
|
O
|
B:OBF190
|
4.9
|
0.0
|
1.0
|
HB3
|
A:LYS136
|
5.0
|
0.0
|
1.0
|
|
Fluorine binding site 2 out
of 2 in 2k1q
Go back to
Fluorine Binding Sites List in 2k1q
Fluorine binding site 2 out
of 2 in the uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of uc(Nmr) Structure of Hepatitis C Virus NS3 Serine Protease Complexed with the Non-Covalently Bound Phenethylamide Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:F190
b:0.0
occ:1.00
|
FG2
|
B:OBF190
|
0.0
|
0.0
|
1.0
|
CG
|
B:OBF190
|
1.4
|
0.0
|
1.0
|
HG
|
B:OBF190
|
2.0
|
0.0
|
1.0
|
FG1
|
B:OBF190
|
2.2
|
0.0
|
1.0
|
CB
|
B:OBF190
|
2.4
|
0.0
|
1.0
|
H2B
|
B:OBF190
|
2.5
|
0.0
|
1.0
|
H
|
A:ALA157
|
2.6
|
0.0
|
1.0
|
O
|
B:GLU188
|
2.7
|
0.0
|
1.0
|
HB3
|
A:ALA157
|
2.8
|
0.0
|
1.0
|
HA
|
A:ALA156
|
2.9
|
0.0
|
1.0
|
N
|
B:OBF190
|
2.9
|
0.0
|
1.0
|
C
|
B:LEU189
|
3.2
|
0.0
|
1.0
|
CA
|
B:OBF190
|
3.2
|
0.0
|
1.0
|
HZ
|
A:PHE154
|
3.2
|
0.0
|
1.0
|
HN
|
B:OBF190
|
3.2
|
0.0
|
1.0
|
H1B
|
B:OBF190
|
3.2
|
0.0
|
1.0
|
N
|
A:ALA157
|
3.3
|
0.0
|
1.0
|
HE2
|
A:PHE154
|
3.4
|
0.0
|
1.0
|
HA
|
B:OBF190
|
3.5
|
0.0
|
1.0
|
O
|
B:LEU189
|
3.5
|
0.0
|
1.0
|
C
|
B:GLU188
|
3.6
|
0.0
|
1.0
|
HG2
|
B:GLU188
|
3.7
|
0.0
|
1.0
|
CB
|
A:ALA157
|
3.7
|
0.0
|
1.0
|
HA
|
B:LEU189
|
3.8
|
0.0
|
1.0
|
CZ
|
A:PHE154
|
3.8
|
0.0
|
1.0
|
CA
|
A:ALA156
|
3.8
|
0.0
|
1.0
|
CA
|
B:LEU189
|
3.9
|
0.0
|
1.0
|
CE2
|
A:PHE154
|
3.9
|
0.0
|
1.0
|
HD3
|
A:LYS136
|
3.9
|
0.0
|
1.0
|
HB3
|
B:GLU188
|
3.9
|
0.0
|
1.0
|
C
|
A:ALA156
|
3.9
|
0.0
|
1.0
|
HB1
|
A:ALA157
|
4.0
|
0.0
|
1.0
|
N
|
B:LEU189
|
4.1
|
0.0
|
1.0
|
CA
|
A:ALA157
|
4.2
|
0.0
|
1.0
|
HB3
|
A:LEU135
|
4.2
|
0.0
|
1.0
|
HA
|
A:LYS136
|
4.3
|
0.0
|
1.0
|
CG
|
B:GLU188
|
4.5
|
0.0
|
1.0
|
CB
|
B:GLU188
|
4.5
|
0.0
|
1.0
|
HB2
|
A:ALA157
|
4.5
|
0.0
|
1.0
|
C
|
B:OBF190
|
4.5
|
0.0
|
1.0
|
HD2
|
A:LYS136
|
4.6
|
0.0
|
1.0
|
HB2
|
A:SER139
|
4.6
|
0.0
|
1.0
|
HB3
|
A:ALA156
|
4.6
|
0.0
|
1.0
|
CA
|
B:GLU188
|
4.7
|
0.0
|
1.0
|
CB
|
A:ALA156
|
4.7
|
0.0
|
1.0
|
CD
|
A:LYS136
|
4.7
|
0.0
|
1.0
|
O
|
A:ARG155
|
4.7
|
0.0
|
1.0
|
HB2
|
A:ALA156
|
4.7
|
0.0
|
1.0
|
HG2
|
A:LYS136
|
4.8
|
0.0
|
1.0
|
OE1
|
B:GLU188
|
4.8
|
0.0
|
1.0
|
N
|
A:ALA156
|
4.9
|
0.0
|
1.0
|
CE1
|
A:PHE154
|
4.9
|
0.0
|
1.0
|
HA
|
A:ALA157
|
5.0
|
0.0
|
1.0
|
H
|
B:GLU188
|
5.0
|
0.0
|
1.0
|
H
|
B:LEU189
|
5.0
|
0.0
|
1.0
|
O
|
A:ALA156
|
5.0
|
0.0
|
1.0
|
|
Reference:
M.Gallo,
M.Pennestri,
M.J.Bottomley,
G.Barbato,
T.Eliseo,
M.Paci,
F.Narjes,
R.De Francesco,
V.Summa,
U.Koch,
R.Bazzo,
D.O.Cicero.
Binding of A Noncovalent Inhibitor Exploiting the S' Region Stabilizes the Hepatitis C Virus NS3 Protease Conformation in the Absence of Cofactor. J.Mol.Biol. V. 385 1142 2009.
ISSN: ISSN 0022-2836
PubMed: 19061898
DOI: 10.1016/J.JMB.2008.11.017
Page generated: Wed Jul 31 15:05:17 2024
|